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Conserved domains on  [gi|212549645|ref|NP_001131114|]
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kinesin-like protein KIF18A [Rattus norvegicus]

Protein Classification

myosin/kinesin family protein( domain architecture ID 366212)

myosin/kinesin family protein; contains an ATPase-containing motor domain found in myosins and kinesins that provides the driving force in myosin and kinesin mediated processes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Motor_domain super family cl22853
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 34-280 2.81e-163

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


The actual alignment was detected with superfamily member cd01370:

Pssm-ID: 473979 [Multi-domain]  Cd Length: 345  Bit Score: 477.22  E-value: 2.81e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  34 VFAYGATGSGKTHTMLGSTAEPGVMYLTMLDLFKCMDEVKDEKECSTAVSYLEVYNEQIRDLLTN-SGPLAVREDAQKGV 112
Cdd:cd01370   98 VFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIRDLLNPsSGPLELREDAQNGI 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 113 VVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDMNAASSRSHAVFQIYLRQQDKTASINQNVHIAKMSLIDLAGSERASI 192
Cdd:cd01370  178 VVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASINQQVRQGKLSLIDLAGSERASA 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 193 SGTKGTRFVEGTNINKSLLALGNVINALADTKRRNQHIPYRNSKLTRLLKDSLGGNCQTIMIAAVSPSSLFYDDTYNTLK 272
Cdd:cd01370  258 TNNRGQRLKEGANINRSLLALGNCINALADPGKKNKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLK 337


                 ....*...
gi 212549645 273 YANRAKDI 280
Cdd:cd01370  338 YANRAKNI 345
 
Name Accession Description Interval E-value
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 34-280 2.81e-163

Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276821 [Multi-domain]  Cd Length: 345  Bit Score: 477.22  E-value: 2.81e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  34 VFAYGATGSGKTHTMLGSTAEPGVMYLTMLDLFKCMDEVKDEKECSTAVSYLEVYNEQIRDLLTN-SGPLAVREDAQKGV 112
Cdd:cd01370   98 VFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIRDLLNPsSGPLELREDAQNGI 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 113 VVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDMNAASSRSHAVFQIYLRQQDKTASINQNVHIAKMSLIDLAGSERASI 192
Cdd:cd01370  178 VVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASINQQVRQGKLSLIDLAGSERASA 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 193 SGTKGTRFVEGTNINKSLLALGNVINALADTKRRNQHIPYRNSKLTRLLKDSLGGNCQTIMIAAVSPSSLFYDDTYNTLK 272
Cdd:cd01370  258 TNNRGQRLKEGANINRSLLALGNCINALADPGKKNKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLK 337


                 ....*...
gi 212549645 273 YANRAKDI 280
Cdd:cd01370  338 YANRAKNI 345
Kinesin pfam00225
Kinesin motor domain;
34-280 1.92e-125

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 378.84  E-value: 1.92e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645   34 VFAYGATGSGKTHTMLGSTAEPGVMYLTMLDLFKCMDEVKDEKECSTAVSYLEVYNEQIRDLL----TNSGPLAVREDAQ 109
Cdd:pfam00225  77 IFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLspsnKNKRKLRIREDPK 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  110 KGVVVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDMNAASSRSHAVFQIYLRQQDKTASINQNVHIAKMSLIDLAGSER 189
Cdd:pfam00225 157 KGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESVKTGKLNLVDLAGSER 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  190 ASISG-TKGTRFVEGTNINKSLLALGNVINALADtkRRNQHIPYRNSKLTRLLKDSLGGNCQTIMIAAVSPSSLFYDDTY 268
Cdd:pfam00225 237 ASKTGaAGGQRLKEAANINKSLSALGNVISALAD--KKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETL 314

                         250
                  ....*....|..
gi 212549645  269 NTLKYANRAKDI 280
Cdd:pfam00225 315 STLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 34-281 1.74e-117

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 358.81  E-value: 1.74e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645    34 VFAYGATGSGKTHTMLGSTAEPGVMYLTMLDLFKCMDEVKDEKECSTAVSYLEVYNEQIRDLL-TNSGPLAVREDAQKGV 112
Cdd:smart00129  83 IFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLnPSSKKLEIREDEKGGV 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645   113 VVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDMNAASSRSHAVFQIYLRQQDKTASiNQNVHIAKMSLIDLAGSERASI 192
Cdd:smart00129 163 YVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSS-SGSGKASKLNLVDLAGSERAKK 241

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645   193 SGTKGTRFVEGTNINKSLLALGNVINALADTKRrNQHIPYRNSKLTRLLKDSLGGNCQTIMIAAVSPSSLFYDDTYNTLK 272
Cdd:smart00129 242 TGAEGDRLKEAGNINKSLSALGNVINALAQHSK-SRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLR 320


                   ....*....
gi 212549645   273 YANRAKDIK 281
Cdd:smart00129 321 FASRAKEIK 329
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
24-429 1.93e-84

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 280.09  E-value: 1.93e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  24 NSAKLSRSLLVFAYGATGSGKTHTMLGSTAEPGVMYLTMLDLFKCMDEVKDEKECSTAVSYLEVYNEQIRDLLTNSGP-L 102
Cdd:COG5059   83 DSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLSPNEEsL 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 103 AVREDAQKGVVVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDMNAASSRSHAVFQIYLRQQDKTASINQNvhiAKMSLI 182
Cdd:COG5059  163 NIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSET---SKLSLV 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 183 DLAGSERASISGTKGTRFVEGTNINKSLLALGNVINALADTKRRNqHIPYRNSKLTRLLKDSLGGNCQTIMIAAVSPSSL 262
Cdd:COG5059  240 DLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG-HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSN 318

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 263 FYDDTYNTLKYANRAKDIKSSQLKSNVVNLSSHISQYvkicnmqKAEILMLKEKLKAYEGQKALTDRNDCAKLVHSNVED 342
Cdd:COG5059  319 SFEETINTLKFASRAKSIKNKIQVNSSSDSSREIEEI-------KFDLSEDRSEIEILVFREQSQLSQSSLSGIFAYMQS 391

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 343 KEIERFQEIlnclfqNREGMRQEYLKVEMLLKENELK---SSYHQQCHK-QIEMMCSEDKLEKATCRRDHRLEKLKSNRC 418
Cdd:COG5059  392 LKKETETLK------SRIDLIMKSIISGTFERKKLLKeegWKYKSTLQFlRIEIDRLLLLREEELSKKKTKIHKLNKLRH 465

                        410
                 ....*....|.
gi 212549645 419 VLEKKKEEMLK 429
Cdd:COG5059  466 DLSSLLSSIPE 476
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 34-282 3.29e-48

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 185.52  E-value: 3.29e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645   34 VFAYGATGSGKTHTMLG----------STAEPGVMYLTMLDLFKCMDE---------VKDEKECstavSYLEVYNEQIRD 94
Cdd:PLN03188  169 VFAYGQTGSGKTYTMWGpanglleehlSGDQQGLTPRVFERLFARINEeqikhadrqLKYQCRC----SFLEIYNEQITD 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645   95 LLTNSGP-LAVREDAQKGVVVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDMNAASSRSHAVFQIYLRQQDK-TASINQ 172
Cdd:PLN03188  245 LLDPSQKnLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKsVADGLS 324

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  173 NVHIAKMSLIDLAGSERASISGTKGTRFVEGTNINKSLLALGNVINALADTKR--RNQHIPYRNSKLTRLLKDSLGGNCQ 250
Cdd:PLN03188  325 SFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgKQRHIPYRDSRLTFLLQESLGGNAK 404

                         250       260       270
                  ....*....|....*....|....*....|..
gi 212549645  251 TIMIAAVSPSSLFYDDTYNTLKYANRAKDIKS 282
Cdd:PLN03188  405 LAMVCAISPSQSCKSETFSTLRFAQRAKAIKN 436
 
Name Accession Description Interval E-value
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 34-280 2.81e-163

Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276821 [Multi-domain]  Cd Length: 345  Bit Score: 477.22  E-value: 2.81e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  34 VFAYGATGSGKTHTMLGSTAEPGVMYLTMLDLFKCMDEVKDEKECSTAVSYLEVYNEQIRDLLTN-SGPLAVREDAQKGV 112
Cdd:cd01370   98 VFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIRDLLNPsSGPLELREDAQNGI 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 113 VVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDMNAASSRSHAVFQIYLRQQDKTASINQNVHIAKMSLIDLAGSERASI 192
Cdd:cd01370  178 VVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASINQQVRQGKLSLIDLAGSERASA 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 193 SGTKGTRFVEGTNINKSLLALGNVINALADTKRRNQHIPYRNSKLTRLLKDSLGGNCQTIMIAAVSPSSLFYDDTYNTLK 272
Cdd:cd01370  258 TNNRGQRLKEGANINRSLLALGNCINALADPGKKNKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLK 337


                 ....*...
gi 212549645 273 YANRAKDI 280
Cdd:cd01370  338 YANRAKNI 345
Kinesin pfam00225
Kinesin motor domain;
34-280 1.92e-125

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 378.84  E-value: 1.92e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645   34 VFAYGATGSGKTHTMLGSTAEPGVMYLTMLDLFKCMDEVKDEKECSTAVSYLEVYNEQIRDLL----TNSGPLAVREDAQ 109
Cdd:pfam00225  77 IFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLspsnKNKRKLRIREDPK 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  110 KGVVVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDMNAASSRSHAVFQIYLRQQDKTASINQNVHIAKMSLIDLAGSER 189
Cdd:pfam00225 157 KGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESVKTGKLNLVDLAGSER 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  190 ASISG-TKGTRFVEGTNINKSLLALGNVINALADtkRRNQHIPYRNSKLTRLLKDSLGGNCQTIMIAAVSPSSLFYDDTY 268
Cdd:pfam00225 237 ASKTGaAGGQRLKEAANINKSLSALGNVISALAD--KKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETL 314

                         250
                  ....*....|..
gi 212549645  269 NTLKYANRAKDI 280
Cdd:pfam00225 315 STLRFASRAKNI 326
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 34-278 4.11e-118

Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276812 [Multi-domain]  Cd Length: 326  Bit Score: 360.03  E-value: 4.11e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  34 VFAYGATGSGKTHTMLGSTAE-PGVMYLTMLDLFKCMDEVKDEK-ECSTAVSYLEVYNEQIRDLL--TNSGPLAVREDAQ 109
Cdd:cd00106   81 IFAYGQTGSGKTYTMLGPDPEqRGIIPRALEDIFERIDKRKETKsSFSVSASYLEIYNEKIYDLLspVPKKPLSLREDPK 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 110 KGVVVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDMNAASSRSHAVFQIYLRQQDKTASINQnVHIAKMSLIDLAGSER 189
Cdd:cd00106  161 RGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGES-VTSSKLNLVDLAGSER 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 190 ASISGTKGTRFVEGTNINKSLLALGNVINALADtkRRNQHIPYRNSKLTRLLKDSLGGNCQTIMIAAVSPSSLFYDDTYN 269
Cdd:cd00106  240 AKKTGAEGDRLKEGGNINKSLSALGKVISALAD--GQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLS 317


                 ....*....
gi 212549645 270 TLKYANRAK 278
Cdd:cd00106  318 TLRFASRAK 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 34-281 1.74e-117

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 358.81  E-value: 1.74e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645    34 VFAYGATGSGKTHTMLGSTAEPGVMYLTMLDLFKCMDEVKDEKECSTAVSYLEVYNEQIRDLL-TNSGPLAVREDAQKGV 112
Cdd:smart00129  83 IFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLnPSSKKLEIREDEKGGV 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645   113 VVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDMNAASSRSHAVFQIYLRQQDKTASiNQNVHIAKMSLIDLAGSERASI 192
Cdd:smart00129 163 YVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSS-SGSGKASKLNLVDLAGSERAKK 241

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645   193 SGTKGTRFVEGTNINKSLLALGNVINALADTKRrNQHIPYRNSKLTRLLKDSLGGNCQTIMIAAVSPSSLFYDDTYNTLK 272
Cdd:smart00129 242 TGAEGDRLKEAGNINKSLSALGNVINALAQHSK-SRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLR 320


                   ....*....
gi 212549645   273 YANRAKDIK 281
Cdd:smart00129 321 FASRAKEIK 329
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 34-281 1.03e-95

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 303.12  E-value: 1.03e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  34 VFAYGATGSGKTHTMLGSTAEPGVMYLTMLDLFKCMDEVKDEK-ECSTAVSYLEVYNEQIRDLLT-----NSGPLAVRED 107
Cdd:cd01365   96 LFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNmSYSVEVSYMEIYNEKVRDLLNpkpkkNKGNLKVREH 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 108 AQKGVVVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDMNAASSRSHAVFQIYLRQQD-KTASINQNVHIAKMSLIDLAG 186
Cdd:cd01365  176 PVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRhDAETNLTTEKVSKISLVDLAG 255

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 187 SERASISGTKGTRFVEGTNINKSLLALGNVINALAD-----TKRRNQHIPYRNSKLTRLLKDSLGGNCQTIMIAAVSPSS 261
Cdd:cd01365  256 SERASSTGATGDRLKEGANINKSLTTLGKVISALADmssgkSKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPAD 335

                        250       260
                 ....*....|....*....|
gi 212549645 262 LFYDDTYNTLKYANRAKDIK 281
Cdd:cd01365  336 INYEETLSTLRYADRAKKIV 355
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 34-281 3.44e-93

Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276823 [Multi-domain]  Cd Length: 341  Bit Score: 295.78  E-value: 3.44e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  34 VFAYGATGSGKTHTMlGSTA-------EPGVMYLTMLDLFKCMDEVKDEKECSTAVSYLEVYNEQIRDLLTNS----GPL 102
Cdd:cd01372   77 VLAYGQTGSGKTYTM-GTAYtaeedeeQVGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDPEtdkkPTI 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 103 AVREDAQKGVVVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDMNAASSRSHAVFQIYLRQQ------DKTASINQNVHI 176
Cdd:cd01372  156 SIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTkkngpiAPMSADDKNSTF 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 177 -AKMSLIDLAGSERASISGTKGTRFVEGTNINKSLLALGNVINALADTKRRNQHIPYRNSKLTRLLKDSLGGNCQTIMIA 255
Cdd:cd01372  236 tSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIA 315

                        250       260
                 ....*....|....*....|....*.
gi 212549645 256 AVSPSSLFYDDTYNTLKYANRAKDIK 281
Cdd:cd01372  316 CVSPADSNFEETLNTLKYANRARNIK 341
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 34-280 1.61e-87

Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276825 [Multi-domain]  Cd Length: 321  Bit Score: 279.99  E-value: 1.61e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  34 VFAYGATGSGKTHTMLGSTAEPGVMYLTMLDLFKCMDEVKDeKECSTAVSYLEVYNEQIRDLLT-NSGPLAVREDAQKGV 112
Cdd:cd01374   76 IFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPD-REFLLRVSYLEIYNEKINDLLSpTSQNLKIRDDVEKGV 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 113 VVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDMNAASSRSHAVFQIYLRQQDKTASINQNVHIAKMSLIDLAGSERASI 192
Cdd:cd01374  155 YVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGTVRVSTLNLIDLAGSERAAQ 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 193 SGTKGTRFVEGTNINKSLLALGNVINALADtKRRNQHIPYRNSKLTRLLKDSLGGNCQTIMIAAVSPSSLFYDDTYNTLK 272
Cdd:cd01374  235 TGAAGVRRKEGSHINKSLLTLGTVISKLSE-GKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLK 313


                 ....*...
gi 212549645 273 YANRAKDI 280
Cdd:cd01374  314 FASRAKKI 321
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
 34-280 2.72e-87

Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276822 [Multi-domain]  Cd Length: 334  Bit Score: 279.73  E-value: 2.72e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  34 VFAYGATGSGKTHTMLGSTAEP---GVMYLTMLDLFKCMDEVKDEKECSTAVSYLEVYNEQIRDLLTN--SGPLAVREDA 108
Cdd:cd01371   85 IFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLGKdqTKRLELKERP 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 109 QKGVVVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDMNAASSRSHAVFQIYLRQQDKTASINQNVHIAKMSLIDLAGSE 188
Cdd:cd01371  165 DTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENHIRVGKLNLVDLAGSE 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 189 RASISGTKGTRFVEGTNINKSLLALGNVINALADTKrrNQHIPYRNSKLTRLLKDSLGGNCQTIMIAAVSPSSLFYDDTY 268
Cdd:cd01371  245 RQSKTGATGERLKEATKINLSLSALGNVISALVDGK--STHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETL 322

                        250
                 ....*....|..
gi 212549645 269 NTLKYANRAKDI 280
Cdd:cd01371  323 STLRYANRAKNI 334
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
24-429 1.93e-84

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 280.09  E-value: 1.93e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  24 NSAKLSRSLLVFAYGATGSGKTHTMLGSTAEPGVMYLTMLDLFKCMDEVKDEKECSTAVSYLEVYNEQIRDLLTNSGP-L 102
Cdd:COG5059   83 DSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLSPNEEsL 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 103 AVREDAQKGVVVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDMNAASSRSHAVFQIYLRQQDKTASINQNvhiAKMSLI 182
Cdd:COG5059  163 NIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSET---SKLSLV 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 183 DLAGSERASISGTKGTRFVEGTNINKSLLALGNVINALADTKRRNqHIPYRNSKLTRLLKDSLGGNCQTIMIAAVSPSSL 262
Cdd:COG5059  240 DLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG-HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSN 318

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 263 FYDDTYNTLKYANRAKDIKSSQLKSNVVNLSSHISQYvkicnmqKAEILMLKEKLKAYEGQKALTDRNDCAKLVHSNVED 342
Cdd:COG5059  319 SFEETINTLKFASRAKSIKNKIQVNSSSDSSREIEEI-------KFDLSEDRSEIEILVFREQSQLSQSSLSGIFAYMQS 391

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 343 KEIERFQEIlnclfqNREGMRQEYLKVEMLLKENELK---SSYHQQCHK-QIEMMCSEDKLEKATCRRDHRLEKLKSNRC 418
Cdd:COG5059  392 LKKETETLK------SRIDLIMKSIISGTFERKKLLKeegWKYKSTLQFlRIEIDRLLLLREEELSKKKTKIHKLNKLRH 465

                        410
                 ....*....|.
gi 212549645 419 VLEKKKEEMLK 429
Cdd:COG5059  466 DLSSLLSSIPE 476
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 34-281 2.39e-80

Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276817 [Multi-domain]  Cd Length: 329  Bit Score: 261.37  E-value: 2.39e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  34 VFAYGATGSGKTHTMLGSTAEPGVMYLTMLDLFKCMDEVKDEKEC-STAVSYLEVYNEQIRDLL-TNSGP---LAVREDA 108
Cdd:cd01366   81 IFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEKGWSyTIKASMLEIYNETIRDLLaPGNAPqkkLEIRHDS 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 109 QKGVV-VQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDMNAASSRSHAVFQIYLRQQDKTasiNQNVHIAKMSLIDLAGS 187
Cdd:cd01366  161 EKGDTtVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQ---TGEISVGKLNLVDLAGS 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 188 ERASISGTKGTRFVEGTNINKSLLALGNVINALAdtkRRNQHIPYRNSKLTRLLKDSLGGNCQTIMIAAVSPSSLFYDDT 267
Cdd:cd01366  238 ERLNKSGATGDRLKETQAINKSLSALGDVISALR---QKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNET 314

                        250
                 ....*....|....
gi 212549645 268 YNTLKYANRAKDIK 281
Cdd:cd01366  315 LNSLRFASKVNSCE 328
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
 34-281 1.21e-73

Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276815 [Multi-domain]  Cd Length: 353  Bit Score: 244.16  E-value: 1.21e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  34 VFAYGATGSGKTHTMLGS-----------TAEPGVMYLTMLDLFKCMDEVKdeKECSTAVSYLEVYNEQIRDLLTNSG-- 100
Cdd:cd01364   86 IFAYGQTGTGKTYTMEGDrspneeytwelDPLAGIIPRTLHQLFEKLEDNG--TEYSVKVSYLEIYNEELFDLLSPSSdv 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 101 --PLAVREDA--QKGVVVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDMNAASSRSHAVFQIYLRQQDKTASINQNVHI 176
Cdd:cd01364  164 seRLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDGEELVKI 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 177 AKMSLIDLAGSERASISGTKGTRFVEGTNINKSLLALGNVINALADtkrRNQHIPYRNSKLTRLLKDSLGGNCQTIMIAA 256
Cdd:cd01364  244 GKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE---RAPHVPYRESKLTRLLQDSLGGRTKTSIIAT 320

                        250       260
                 ....*....|....*....|....*
gi 212549645 257 VSPSSLFYDDTYNTLKYANRAKDIK 281
Cdd:cd01364  321 ISPASVNLEETLSTLEYAHRAKNIK 345
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 34-280 9.33e-73

Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276820 [Multi-domain]  Cd Length: 325  Bit Score: 241.08  E-value: 9.33e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  34 VFAYGATGSGKTHTMLGSTAEPGVMYL------TMLDLFKCMDEvkdEKECSTAVSYLEVYNEQIRDLLTNS-GPLAVRE 106
Cdd:cd01369   80 IFAYGQTSSGKTYTMEGKLGDPESMGIiprivqDIFETIYSMDE---NLEFHVKVSYFEIYMEKIRDLLDVSkTNLSVHE 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 107 DAQKGVVVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDMNAASSRSHAVFQIYLRQQDKTASINQNvhiAKMSLIDLAG 186
Cdd:cd01369  157 DKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKS---GKLYLVDLAG 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 187 SERASISGTKGTRFVEGTNINKSLLALGNVINALADTKRrnQHIPYRNSKLTRLLKDSLGGNCQTIMIAAVSPSSLFYDD 266
Cdd:cd01369  234 SEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK--THIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESE 311

                        250
                 ....*....|....
gi 212549645 267 TYNTLKYANRAKDI 280
Cdd:cd01369  312 TLSTLRFGQRAKTI 325
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 34-278 4.45e-71

Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276818 [Multi-domain]  Cd Length: 328  Bit Score: 236.42  E-value: 4.45e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  34 VFAYGATGSGKTHTMLGS----TAEPGVMYLTMLDLFKCMDEVKDEKECSTAVSYLEVYNEQIRDLLTNSGPLAVREDAQ 109
Cdd:cd01367   87 CFAYGQTGSGKTYTMGGDfsgqEESKGIYALAARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLLNRKKRVRLREDGK 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 110 KGVVVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDMNAASSRSHAVFQIYLRqqdktaSINQNVHIAKMSLIDLAGSER 189
Cdd:cd01367  167 GEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILR------DRGTNKLHGKLSFVDLAGSER 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 190 AS--ISGTKGTRfVEGTNINKSLLALGNVINALADTKRrnqHIPYRNSKLTRLLKDSL-GGNCQTIMIAAVSPSSLFYDD 266
Cdd:cd01367  241 GAdtSSADRQTR-MEGAEINKSLLALKECIRALGQNKA---HIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEH 316

                        250
                 ....*....|..
gi 212549645 267 TYNTLKYANRAK 278
Cdd:cd01367  317 TLNTLRYADRVK 328
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 34-278 7.93e-68

Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276827 [Multi-domain]  Cd Length: 319  Bit Score: 227.39  E-value: 7.93e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  34 VFAYGATGSGKTHTMLGSTAEPGVMYLTMLDLFKCMDevKDEKECSTAVSYLEVYNEQIRDLLT-NSGPLAVREDAQKGV 112
Cdd:cd01376   81 VFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTR--KEAWALSFTMSYLEIYQEKILDLLEpASKELVIREDKDGNI 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 113 VVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDMNAASSRSHAVFQIYLRQQDKTASINQNVhiAKMSLIDLAGSERASI 192
Cdd:cd01376  159 LIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQRT--GKLNLIDLAGSEDNRR 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 193 SGTKGTRFVEGTNINKSLLALGNVINALADTKRRnqhIPYRNSKLTRLLKDSLGGNCQTIMIAAVSPSSLFYDDTYNTLK 272
Cdd:cd01376  237 TGNEGIRLKESGAINSSLFVLSKVVNALNKNLPR---IPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLN 313


                 ....*.
gi 212549645 273 YANRAK 278
Cdd:cd01376  314 FAARSR 319
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 34-278 2.70e-64

Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276826 [Multi-domain]  Cd Length: 334  Bit Score: 218.60  E-value: 2.70e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  34 VFAYGATGSGKTHTMLGST---AEPGVMYLTMLDLFKCMDEvKDEKECSTAVSYLEVYNEQIRDLLT-------NSGPLA 103
Cdd:cd01375   84 IFAYGQTGAGKTFTMTGGTenyKHRGIIPRALQQVFRMIEE-RPTKAYTVHVSYLEIYNEQLYDLLStlpyvgpSVTPMT 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 104 VREDAQKGVVVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDMNAASSRSHAVFQIYLRQQDKTASINQNVHiAKMSLID 183
Cdd:cd01375  163 ILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRTLSSEKYIT-SKLNLVD 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 184 LAGSERASISGTKGTRFVEGTNINKSLLALGNVINALADTKRrnQHIPYRNSKLTRLLKDSLGGNCQTIMIAAVSPSSLF 263
Cdd:cd01375  242 LAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQ 319

                        250
                 ....*....|....*
gi 212549645 264 YDDTYNTLKYANRAK 278
Cdd:cd01375  320 LEETLSTLRFASRVK 334
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 34-281 6.80e-63

Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276824 [Multi-domain]  Cd Length: 347  Bit Score: 215.06  E-value: 6.80e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  34 VFAYGATGSGKTHTMLG--------STAEPGVMYLTMLDLFKCMD----EVKDEKECSTAVSYLEVYNEQIRDLL-TNSG 100
Cdd:cd01373   78 IFAYGQTGSGKTYTMWGpsesdnesPHGLRGVIPRIFEYLFSLIQrekeKAGEGKSFLCKCSFLEIYNEQIYDLLdPASR 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 101 PLAVREDAQKGVVVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDMNAASSRSHAVFQIYLRQQDKTASINqNVHIAKMS 180
Cdd:cd01373  158 NLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKACFV-NIRTSRLN 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 181 LIDLAGSERASISGTKGTRFVEGTNINKSLLALGNVINALADTKR-RNQHIPYRNSKLTRLLKDSLGGNCQTIMIAAVSP 259
Cdd:cd01373  237 LVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHgKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHP 316

                        250       260
                 ....*....|....*....|..
gi 212549645 260 SSLFYDDTYNTLKYANRAKDIK 281
Cdd:cd01373  317 SSKCFGETLSTLRFAQRAKLIK 338
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 30-278 4.86e-61

Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276819 [Multi-domain]  Cd Length: 345  Bit Score: 209.94  E-value: 4.86e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  30 RSLLVFAYGATGSGKTHTMLGSTAEPGVMYLTMLDLFKCMdevkdeKECSTAVSYLEVYNEQIRDLLTNSG--------P 101
Cdd:cd01368   88 KNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSI------GGYSVFVSYIEIYNEYIYDLLEPSPssptkkrqS 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 102 LAVREDAQKGVVVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDMNAASSRSHAVFQIYLRQQ--DKTASINQ---NVHI 176
Cdd:cd01368  162 LRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQApgDSDGDVDQdkdQITV 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 177 AKMSLIDLAGSERASISGTKGTRFVEGTNINKSLLALGNVINALAD--TKRRNQHIPYRNSKLTRLLKDSLGGNCQTIMI 254
Cdd:cd01368  242 SQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLREnqLQGTNKMVPFRDSKLTHLFQNYFDGEGKASMI 321

                        250       260
                 ....*....|....*....|....
gi 212549645 255 AAVSPSSLFYDDTYNTLKYANRAK 278
Cdd:cd01368  322 VNVNPCASDYDETLHVMKFSAIAQ 345
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 34-282 3.29e-48

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 185.52  E-value: 3.29e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645   34 VFAYGATGSGKTHTMLG----------STAEPGVMYLTMLDLFKCMDE---------VKDEKECstavSYLEVYNEQIRD 94
Cdd:PLN03188  169 VFAYGQTGSGKTYTMWGpanglleehlSGDQQGLTPRVFERLFARINEeqikhadrqLKYQCRC----SFLEIYNEQITD 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645   95 LLTNSGP-LAVREDAQKGVVVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDMNAASSRSHAVFQIYLRQQDK-TASINQ 172
Cdd:PLN03188  245 LLDPSQKnLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKsVADGLS 324

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  173 NVHIAKMSLIDLAGSERASISGTKGTRFVEGTNINKSLLALGNVINALADTKR--RNQHIPYRNSKLTRLLKDSLGGNCQ 250
Cdd:PLN03188  325 SFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgKQRHIPYRDSRLTFLLQESLGGNAK 404

                         250       260       270
                  ....*....|....*....|....*....|..
gi 212549645  251 TIMIAAVSPSSLFYDDTYNTLKYANRAKDIKS 282
Cdd:PLN03188  405 LAMVCAISPSQSCKSETFSTLRFAQRAKAIKN 436
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 34-219 5.25e-14

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 70.84  E-value: 5.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645  34 VFAYGATGSGKTHTMLGStaepgVMYLTmldlfkcmdevkdekecstavsylEVYNEQIRDLLTNSGplavredaqkgvv 113
Cdd:cd01363   55 IFAYGESGAGKTETMKGV-----IPYLA------------------------SVAFNGINKGETEGW------------- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212549645 114 vQGLTLHQPKSSEEILQLLDNGNKNRTQhPTDMNAASSRSHAVFQIylrqqdktasinqnvhiakmsLIDLAGSERasis 193
Cdd:cd01363   93 -VYLTEITVTLEDQILQANPILEAFGNA-KTTRNENSSRFGKFIEI---------------------LLDIAGFEI---- 145

                        170       180
                 ....*....|....*....|....*.
gi 212549645 194 gtkgtrfvegtnINKSLLALGNVINA 219
Cdd:cd01363  146 ------------INESLNTLMNVLRA 159
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
 34-96 6.41e-04

Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 40.67  E-value: 6.41e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212549645   34 VFAYGATGSGKTHTMLGSTAEpgvmyltmlDLFKCMDEVKDEKECSTAVSYLEVYNEQIRDLL 96
Cdd:pfam16796  91 IFAYGQTGSGSNDGMIPRARE---------QIFRFISSLKKGWKYTIELQFVEIYNESSQDLL 144
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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